Chloroperoxidase halogenation reactions. Chemical versus enzymic halogenating intermediates.

Libby, R. Daniel; Thomas, John A.; Kaiser, Lothar; Hager, Lowell P.

doi:10.1016/s0021-9258(18)34630-1

Cited by 167 publications

(47 citation statements)

References 33 publications

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“…Chloroperoxidase (CPO, EC 1.11.1.10) from the filamentous fungus Caldariomyces fumago is a versatile heme-dependent peroxidase requiring hydrogen peroxide and chloride, bromide or iodide for the halogenation of organic substrates suitable for electrophilic attack. 4 CPO catalyses the halogenation of different molecules such as aromatic hydrocarbons, 5,6 monoterpenes, 7 lignin structures 8 or flavanones. 9 In addition to halogenations CPO catalyses hydrogen peroxide-supported oxidation, the dismutation of hydrogen peroxide (catalase reaction), and some cytochrome P450 monooxygenase-like reactions.…”

Section: Introductionmentioning

confidence: 99%

Gas diffusion electrode as novel reaction system for an electro-enzymatic process with chloroperoxidase

et al. 2011

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Section: Introductionmentioning

confidence: 99%

Gas diffusion electrode as novel reaction system for an electro-enzymatic process with chloroperoxidase

et al. 2011

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“…In a few instances, compound I is apparently reduced directly to the ferric form in a two-electron transfer process (Nakamura et al, 1985), depending upon the nature of the substrate. Chloroperoxidase (CPO),* 1 besides being able to function like other heme-containing peroxidases, is able to catalyze a number of reactions that were believed to be typical of catalases (Thomas et al, 1970;Araiso et al, 1981) and to utilize chloride and bromide ions as donors for halogenation reactions (Hewson & Hager, 1978;Libby et al, 1982). More recently, CPO has been found to be capable of some P-450-type reactions such as the N-dealkylation of alkylamines (Kedderis & Hollenberg, 1983; Kedderis et al, 1986) and the epoxidation of alkenes (Me Carthy & White, 1983; Ortiz de Montellano et al, 1987).…”

mentioning

confidence: 99%

Mechanism of enantioselective oxygenation of sulfides catalyzed by chloroperoxidase and horseradish peroxidase. Spectral studies and characterization of enzyme-substrate complexes

Casella

Gullotti²,

Ghezzi³

et al. 1992

Biochemistry

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The binding of a series of alkyl aryl sulfides to chloroperoxidase (CPO) and horseradish peroxidase (HRP) has been investigated by optical difference spectroscopy, circular dichroism, paramagnetic NMR spectroscopy, and NMR relaxation measurements. The data are consistent with binding of the sulfides in the distal side of the heme pocket with CPO and near the heme edge with HRP. A linear correlation between the binding constants of para-substituted sulfides to CPO and the Taft sigma I parameter suggests that these substrates act as donors in donor-acceptor complexes involving some residue of the protein chain. Spectral studies during turnover show that high enantioselectivity in the CPO-catalyzed oxidation of sulfides results from a reaction pathway that does not involve the accumulation of compound II enzyme intermediate.

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“…The enzymatic activity of chloroperoxidase has been extensively studied by different research groups in late nineteenth century. [15,[109][110][111][112][113] In general, the enzymatic activity of CPO proceeds with the initial oxidation of the active site of iron(III)porphyrin A by H 2 O 2 to form an iron(IV)oxo species B (Scheme 11). Thereafter, B interacts with the halide source to form iron(III) hypohalite intermediate C which interacts with the substrates to give the halogenated product and an iron(III)hydroxy species D followed by its conversion to A.…”

Section: Metal-porphyrin Based Systemmentioning

confidence: 99%

“…The naturally occurring metal‐porphyrin based halogenating catalyst is chloroperoxidase (CPO) enzyme possessing an iron(III) porphyrin in its native structure. The enzymatic activity of chloroperoxidase has been extensively studied by different research groups in late nineteenth century [15,109–113] . In general, the enzymatic activity of CPO proceeds with the initial oxidation of the active site of iron(III)porphyrin A by H 2 O 2 to form an iron(IV)oxo species B (Scheme 11).…”

Section: Bio‐inspired C−h Halogenation By High‐valent 3 D Metal‐oxo C...mentioning

confidence: 99%

Recent Advances in First‐Row Transition‐Metal‐Mediated C−H Halogenation of (Hetero)arenes and Alkanes

et al. 2022

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The ubiquity of carbon halogen bonds in the structural core of numerous biomolecules and pharmaceuticals along with their role as synthetic precursors in various organic reactions makes the organic halides a crucial class of organic compounds. Consequently, the synthesis of organic halides with high regioselectivity is of paramount importance in synthetic chemistry. In nature, selective halogenation is achieved by metalloenzymes with high efficiency involving high-valent iron-oxo as active species. The high selectivity of halogenating enzymes attracted considerable attention leading to the development of several biomimetic approaches for CÀ H halogenation. Moreover, the emergence of transition metal (TM) catalyzed site-selective CÀ H halogenation protocols through the development of several directed strategies has also been impressive. There has been significant development in the first row TM catalyzed CÀ H halogenation reactions despite the dominance of late transition metals catalysts in this field. But in literature, there is no up-to-date recent review article that consolidates bio-mimetic as well as synthetic strategies of CÀ H halogenation (X = Cl, Br, I) containing organo-fluorination with all the first-row transition metals. Thus, we got motivated and have focused to elucidate the recent developments of first row TM-catalyzed CÀ H halogenation of (hetero)arenes and alkanes through biomimetic approaches as well as directed and undirected strategies in this present review. Additionally, this review covers the recent progresses in the CÀ H fluorination methodologies. Altogether, the review will provide a combined overview of all the strategies of first-row transition-metalmediated CÀ H halogenation reactions that may benefit the scientific community towards the development of new methodologies in this field.

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Chloroperoxidase halogenation reactions. Chemical versus enzymic halogenating intermediates.

Cited by 167 publications

References 33 publications

Gas diffusion electrode as novel reaction system for an electro-enzymatic process with chloroperoxidase

Gas diffusion electrode as novel reaction system for an electro-enzymatic process with chloroperoxidase

Mechanism of enantioselective oxygenation of sulfides catalyzed by chloroperoxidase and horseradish peroxidase. Spectral studies and characterization of enzyme-substrate complexes

Recent Advances in First‐Row Transition‐Metal‐Mediated C−H Halogenation of (Hetero)arenes and Alkanes

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